Purification and partial characterization of a bacteriocin isolated from <i>Bacteroides ovatus</i> H47

Miranda, Cláudia Madeira; Farias, Luiz M.; Carvalho, Maria Auxiliadora Roque de; Damasceno, Carlos Américo Veiga; Tótola, Antônio Helvécio; Tavares, Carlos A. P.; Cisalpino, E. O.; Vieira, Eliane

doi:10.1139/m93-023

Cited by 17 publications

(8 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Production of antimicrobial proteins by intestinal Bacteroides species has been reported, with the most recent study in 1999 (Miranda et al ., ; Farias et al ., ; Papastathopoulou et al ., ; Avelar et al ., ). However, no responsible gene was cloned nor was the protein purified, therefore, the identity of these molecules remains unknown.…”

Section: Introductionmentioning

confidence: 98%

An antimicrobial protein of the gut symbiont Bacteroides fragilis with a MACPF domain of host immune proteins

Chatzidaki‐Livanis

Coyne

Comstock

2014

Molecular Microbiology

View full text Add to dashboard Cite

Summary Bacteroidales are the most abundant Gram negative bacteria of the human intestinal microbiota comprising more than half of the bacteria in many individuals. Some of the factors that these bacteria use to establish and maintain themselves in this ecosystem are beginning to be identified. However, ecological competition, especially interference competition where one organism directly harms another, is largely unexplored. To begin to understand the relevance of this ecological principle as it applies to these abundant gut bacteria and factors that may promote such competition, we screened Bacteroides fragilis for the production of antimicrobial molecules. We found that the production of extracellularly secreted antimicrobial molecules is widespread in this species. The first identified molecule, described in this manuscript, contains a membrane attack complex/perforin (MACPF) domain present in host immune molecules that kill bacteria and virally infected cells by pore formation, and mutations affecting key residues of this domain abrogated its activity. This antimicrobial molecule, termed BSAP-1, is secreted from the cell in outer membrane vesicles and no additional proteins are required for its secretion, processing or immunity of the producing cell. This study provides the first insight into secreted molecules that promote competitive interference among Bacteroidales strains of the human gut.

show abstract

Section: Introductionmentioning

confidence: 98%

An antimicrobial protein of the gut symbiont Bacteroides fragilis with a MACPF domain of host immune proteins

Chatzidaki‐Livanis

Coyne

Comstock

2014

Molecular Microbiology

View full text Add to dashboard Cite

show abstract

“…Bacteriocin production is a common attribute in many Gram-positive bacteria. Bacteriocins and bacteriocin-like substances have been described for a number of strict anaerobes (Barefoot and Klaenhammer 1984;Garnier and Cole 1988;Miranda et al 1993) and facultative anaerobes (Iverson and Millis 1976;Arihara et al 1993;Laukova et al 1998a) isolated from nonruminant anaerobic sources.…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of a bacteriocin-like compound (Lichenin) produced anaerobically by Bacillus licheniformis isolated from water buffalo

et al. 2001

View full text Add to dashboard Cite

Aims: To characterize a bacteriocin‐like factor from Bacillus licheniformis 26 L‐10/3RA isolated from buffalo rumen. Methods and Results: The culture supernatant exhibited the antibacterial activity against a number of indicator organisms in a cut‐well agar assay under anaerobic conditions. The inhibitory component was purified by following ammonium sulphate precipitation, gel filtration and ion exchange chromatography and confirmed to be a single peptide. A single band on tricine‐sodium dodecyl sulphate‐polyacrylamide gel electrophoresis confirmed that the peptide was purified to homogeneity and having an estimated molecular mass of approximately 1400 dalton. Complete amino acid sequence of the peptide yielded 12 amino acids from the N‐terminal end (ISLEICXIFHDN). No homology with previously reported bacteriocins was observed and has been designated as Lichenin. Lichenin was found to be hydrophobic, sensitive to atmospheric oxygen, retained biological activity even after boiling for 10 min and was active over a pH range of 4·0–9·0. Conclusions: The Lichenin represents the first anaerobiosis specific expression of bacteriocin‐like compound isolated from Bacillus licheniformis 26 L‐10/3RA of buffalo rumen origin. Significance and Impact of the Study: Lichenin could be a potential condidate for manipulating the rumen function at molecular level intended for improving the productivity of the ruminant.

show abstract

“…Bacteriocins and bacteriocin-like activities have been described for a number of strict anaerobes (5,11,39,40,47) and facultative anaerobes (2,23,35,54) isolated from nonruminal anaerobic sources. In many cases, related organisms have been isolated from the rumen (49).…”

mentioning

confidence: 99%

Isolation and characterization of a bacteriocin (Butyrivibriocin AR10) from the ruminal anaerobe Butyrivibrio fibrisolvens AR10: evidence in support of the widespread occurrence of bacteriocin-like activity among ruminal isolates of B. fibrisolvens

Kalmokoff

Teather

1997

Appl Environ Microbiol

View full text Add to dashboard Cite

Forty-nine isolates of Butyrivibrio fibrisolvens and a single isolate of Butyrivibrio crossotus were screened for the production of inhibitors by a deferred plating procedure. Twenty-five isolates produced factors which, to various degrees, inhibited the growth of the other Butyrivibrio isolates. None of the inhibitory activity was due to bacteriophages. The inhibitory products from 18 of the producing strains were sensitive to protease digestion. Differences in the ranges of activity among the Butyrivibrio isolates and protease sensitivity profiles suggest that a number of different inhibitory compounds are produced. These findings suggest that the production of bacteriocin-like inhibitors may be a widespread characteristic throughout the genus Butyrivibrio. The bacteriocin-like activity from one isolate, B. fibrisolvens AR10, was purified and confirmed to reside in a single peptide. Crude bacteriocin extracts were prepared by ammonium sulfate and methanol precipitation of spent culture supernatants, followed by dialysis and high-speed centrifugation. The active component was isolated from the semicrude extract by reverse-phase chromatography. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis confirmed that the peptide was purified to homogeneity, having an estimated molecular mass of approximately 4,000 Da. The N terminus of the peptide was blocked. A cyanogen bromide cleavage fragment of the native peptide yielded a sequence of 20 amino acids [(M)GIQLAPAXYQDIVNXVA AG]. No homology with previously reported bacteriocins was found. Butyrivibriocin AR10 represents the first bacteriocin isolated from a ruminal anaerobe.

show abstract

Purification and partial characterization of a bacteriocin isolated from Bacteroides ovatus H47

Cited by 17 publications

References 26 publications

An antimicrobial protein of the gut symbiont Bacteroides fragilis with a MACPF domain of host immune proteins

An antimicrobial protein of the gut symbiont Bacteroides fragilis with a MACPF domain of host immune proteins

Purification and characterization of a bacteriocin-like compound (Lichenin) produced anaerobically by Bacillus licheniformis isolated from water buffalo

Isolation and characterization of a bacteriocin (Butyrivibriocin AR10) from the ruminal anaerobe Butyrivibrio fibrisolvens AR10: evidence in support of the widespread occurrence of bacteriocin-like activity among ruminal isolates of B. fibrisolvens

Contact Info

Product

Resources

About